In:
FEBS Letters, Wiley, Vol. 360, No. 2 ( 1995-02-27), p. 211-215
Abstract:
Fraction A of the armadillo submandibular glycoprotein (ASG‐A) is one of the simplest glycoproteins among mammalian salivary mucins. The carbohydrate side chains of this mucous glycoprotein have one‐third of the NeuAc α 2→6GalNAc (sialyl‐Tn) sequence and two thirds of Tn (GalNAc α →Ser/Thr) residues. Those of the desialylated product (ASG‐Tn) are almost exclusively unsubstituted GalNAc residues (Tn determinant). When the binding properties of these glycoproteins were tested by a precipitin assay with Gal, GalNAc and GlcNAc specific lectins, it was found that ASG‐Tn reacted strongly with all of the Tn‐active lectins and completely precipitated Vicia villosa (VVL both B 4 and mixture of A and B), Maclura pomifera (MPA), and Artocarpus integrifolia (jacalin) lectins. However, it precipitated poorly or negligibly with Ricinus communis (RCA 1 ); Dolichos biflorus (DBA); Viscum album , ML‐1; Arachis hypogaea (PNA), and Triticum vulgaris (WGA). The reactivity of ASG‐A (sialyl‐Tn) was as active as that of ASG‐Tn with MPA and less or slightly less active than that of ASG‐Tn with VVL‐A+B, VVLB 4 , HPA, WFA, and jacalin, as one‐third of its Tn was sialylated. These findings indicate that ASG‐A and its desialylated product (ASG‐Tn) are highly useful reagents for the differentiation of Tn, T (Gal β 1→3GalNAc), A (GalNAc α 1→3Gal) or Gal specific lectins and monoclonal antibodies against such epitopes.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(95)00106-J
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1460391-3
SSG:
12
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